Phosphorylation of type-1 inositol 1,4,5-trisphosphate receptors by cyclic nucleotide-dependent protein kinases: a mutational analysis of the functionally important sites in the S2+ and S2- splice variants.

doi:10.1074/jbc.M306270200

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Article

Phosphorylation of type-1 inositol 1,4,5-trisphosphate receptors by cyclic nucleotide-dependent protein kinases: a mutational analysis of the functionally important sites in the S2+ and S2- splice variants.

The Journal of biological chemistry - 14 Nov 2003

Wagner Larry E, Li Wen-Hong, Yule David I

Abstract excerpt

Inositol 1,4,5-trisphosphate receptors (InsP3R) are the major route of intracellular calcium release in eukaryotic cells and as such are pivotal for stimulation of Ca2+-dependent effectors important for numerous physiological processes. Modulation of this release has important consequences for defining the particular spatio-temporal characteristics of Ca2+ signals. In this study, regulation of Ca2+ release by...

Topics

Alternative Splicing
Animals
Calcium
Calcium Channels
Chickens
Cyclic AMP-Dependent Protein Kinases
Cyclic GMP-Dependent Protein Kinases
Cyclic Nucleotide-Regulated Protein Kinases
DNA Mutational Analysis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Inositol 1,4,5-Trisphosphate Receptors

Mutation

Neurons

Phosphorylation

Photolysis

Receptors, Cytoplasmic and Nuclear

Serine

Time Factors

Transfection

Source

Open in PubMed

Identifiers

PMID: 12939273
DOI: 10.1074/jbc.M306270200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-12939273-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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